ID   NOS2_BOVIN              Reviewed;        1156 AA.
AC   Q27995; Q06Q84; Q27985;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 3.
DT   08-NOV-2023, entry version 159.
DE   RecName: Full=Nitric oxide synthase, inducible;
DE            EC=1.14.13.39 {ECO:0000250|UniProtKB:P35228};
DE   AltName: Full=Inducible NO synthase;
DE            Short=Inducible NOS;
DE            Short=iNOS;
DE   AltName: Full=NOS type II;
DE            Short=NOSII;
DE   AltName: Full=Peptidyl-cysteine S-nitrosylase NOS2;
GN   Name=NOS2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Widdison S., Ashley G.R., Howard C.J., Coffey T.J.;
RT   "Cloning and characterization of bovine inducible nitric oxide synthase.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 166-275.
RC   TISSUE=Bone marrow macrophage;
RX   PubMed=7536776;
RA   Adler H., Frech B., Thoeny M., Pfister H., Peterhans E., Jungi T.W.;
RT   "Inducible nitric oxide synthase in cattle. Differential cytokine
RT   regulation of nitric oxide synthase in bovine and murine macrophages.";
RL   J. Immunol. 154:4710-4718(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 987-1122.
RC   TISSUE=Pulmonary artery;
RX   PubMed=7558036; DOI=10.1006/geno.1995.1086;
RA   Bloch K.D., Wolfram J.R., Brown D.M., Roberts J.D. Jr., Zapol D.G.,
RA   Lepore J.J., Filippov G., Thomas J.E., Jacob H.J., Bloch D.B.;
RT   "Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B,
RT   and NOS2C) colocalize to human chromosome 17.";
RL   Genomics 27:526-530(1995).
CC   -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC       diverse functions throughout the body. In macrophages, NO mediates
CC       tumoricidal and bactericidal actions. Also has nitrosylase activity and
CC       mediates cysteine S-nitrosylation of cytoplasmic target proteins such
CC       PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex
CC       involved in the selective inflammatory stimulus-dependent S-
CC       nitrosylation of GAPDH implicated in regulation of the GAIT complex
CC       activity and probably multiple targets including ANXA5, EZR, MSN and
CC       VIM. Involved in inflammation, enhances the synthesis of pro-
CC       inflammatory mediators such as IL6 and IL8.
CC       {ECO:0000250|UniProtKB:P35228, ECO:0000250|UniProtKB:P79290}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC         + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC         Evidence={ECO:0000250|UniProtKB:P35228};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC         Evidence={ECO:0000250|UniProtKB:P35228};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P35228};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P29476};
CC       Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P35228};
CC       Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P35228};
CC   -!- COFACTOR:
CC       Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC         Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:P35228};
CC       Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC       enzyme. {ECO:0000250|UniProtKB:P35228};
CC   -!- ACTIVITY REGULATION: Regulated by calcium/calmodulin. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with NHERF1. Interacts with GAPDH;
CC       induced by oxidatively-modified low-densitity lipoprotein (LDL(ox)).
CC       Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9
CC       transnitrosylase complex. Interacts with SPSB1, SPSB2 and SPSB4.
CC       Interacts with ELOC and CUL5 in the presence of SPSB1 or SPSB2 or
CC       SPSB4. Forms a complex with ASL, ASS1 and HSP90AA1; the complex
CC       regulates cell-autonomous L-arginine synthesis and citrulline recycling
CC       while channeling extracellular L-arginine to nitric oxide synthesis
CC       pathway. {ECO:0000250|UniProtKB:P29477}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P35228}. Note=Localizes as discrete foci
CC       scattered throughout the cytosol and in the presence of SPSB1 and
CC       SPSB4, exhibits a more diffuse cytosolic localization.
CC       {ECO:0000250|UniProtKB:P35228}.
CC   -!- PTM: Polyubiquitinated; mediated by SPSB1, SPSB2 and SPSB4, leading to
CC       proteasomal degradation. {ECO:0000250|UniProtKB:P35228}.
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR   EMBL; DQ676956; ABG74910.1; -; mRNA.
DR   EMBL; U14640; AAC48470.2; -; mRNA.
DR   EMBL; U18331; AAC48479.1; -; mRNA.
DR   PIR; I46074; I46074.
DR   RefSeq; NP_001070267.1; NM_001076799.1.
DR   AlphaFoldDB; Q27995; -.
DR   SMR; Q27995; -.
DR   STRING; 9913.ENSBTAP00000009062; -.
DR   PaxDb; 9913-ENSBTAP00000009062; -.
DR   GeneID; 282876; -.
DR   KEGG; bta:282876; -.
DR   CTD; 4843; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   InParanoid; Q27995; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004517; F:nitric-oxide synthase activity; ISS:UniProtKB.
DR   GO; GO:0006527; P:arginine catabolic process; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IBA:GO_Central.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
DR   GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; ISS:UniProtKB.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR   GO; GO:0032310; P:prostaglandin secretion; ISS:UniProtKB.
DR   GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR   GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR   CDD; cd00795; NOS_oxygenase_euk; 1.
DR   Gene3D; 3.40.50.360; -; 2.
DR   Gene3D; 6.10.250.410; -; 1.
DR   Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR044943; NOS_dom_1.
DR   InterPro; IPR044940; NOS_dom_2.
DR   InterPro; IPR044944; NOS_dom_3.
DR   InterPro; IPR012144; NOS_euk.
DR   InterPro; IPR004030; NOS_N.
DR   InterPro; IPR036119; NOS_N_sf.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR   PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF02898; NO_synthase; 1.
DR   PIRSF; PIRSF000333; NOS; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS60001; NOS; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calmodulin-binding; Cytoplasm; FAD; Flavoprotein; FMN; Heme; Iron;
KW   Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Ubl conjugation; Zinc.
FT   CHAIN           1..1156
FT                   /note="Nitric oxide synthase, inducible"
FT                   /id="PRO_0000170926"
FT   DOMAIN          539..677
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          730..970
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          27..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..535
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   MOTIF           23..27
FT                   /note="DINNN-motif; mediates interaction with SPSB1, SPSB2
FT                   and SPSB4"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   COMPBIAS        27..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         118
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         200
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         263
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         372
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         373
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         377
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         381
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         462
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         463
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         476
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         491
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         545
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         546
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         547
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         549
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         550
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         591
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         592
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         628
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         635
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         661
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         665
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         750
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         772
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         906
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         908
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         909
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         924
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         926
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         929
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         930
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         943
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         944
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         945
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         984
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1017
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1046
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1047
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1053
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1055
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1057
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1090
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   MOD_RES         575
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06518"
FT   CONFLICT        236
FT                   /note="N -> S (in Ref. 2; AAC48470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1068..1069
FT                   /note="VL -> AF (in Ref. 3; AAC48479)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1156 AA;  131208 MW;  52A52C984462F692 CRC64;
     MACPWQFLFK IKSQKVDLAT ELDINNNVGK FYQPPSSPVT QDDPKRHSPG KHGNESPQPL
     TGTVKTSPES LSKLDAPPSA CPRHVRIKNW GSGVTFQDTL HQKAKGDLSC KSKSCLASIM
     NPKSLTIGPR DKPTPPDELL PQAIEFVNQY YGSFKEAKIE EHLARVEAVT KEIETTGTYQ
     LTGDELIFAT KQAWRNAPRC IGRIQWSNLQ VFDARSCSTA QEMFEHICRH VRYATNNGNI
     RSAITVFPQR SDGKHDFRVW NAQLIRYAGY QMPDGSIRGD PANVEFTQLC IDLGWKPKYG
     RFDVLPLVLQ ADGRDPELFE IPPDLVLEVP MEHPRYEWFR ELELKWYALP AVANMLLEVG
     GLEFPGCPFN GWYMGTEVGV RDFCDAQRYN ILEEVGRRMG LETHKVASLW KDRAVVEINV
     AVLHSFQKQN VTIMDHHSAA ESFMKYMQNE YRSRGGCPAD WIWLVPPISG SITPVFHQEM
     LNYVLSPFYY YQVEPWKTHV WQDERRRPQR REIRFKVLVK AVFFASVLMH KAMASRVRAT
     ILFATETGRS ETLAQDLGAL FSCAFNPKVL CMDQYQLSHL EEEQLLLVVT STFGNGDSPG
     NGEKLKKSLL MLKELTNTFR YAVFGLGSSM YPQFCAFAHD IDQKLSQLGA SQLAPTGEGD
     ELSGQEEAFR SWAVQTFKAA CETFDVSGKH HIEIPKLYTS NVTWDPQHYR LVQDSEPLDL
     NKALSSMHAK HVFTMRLKSQ QNLQSPKSSR TTLLVELSCE GSQAPSYLPG EHLGVFPCNQ
     PALVQGILER VVDGPAPHQP VRLETLCENG SYWVKDKRLP PCSLSQALTY FLDITTPPTQ
     LLLRKLAQLA TEEAEKQRLE TLCQPSDYNK WKFTNSPTFL EVLEEFPSLR VSASFLLSQL
     PILKPRYYSI SSSRDLTPTE IHLTVAVLTY RTRDGQGPLH HGVCSTWLSS LKPQDPVPCF
     VRSASGFQLP EDRSRPCILI GPGTGIAPFR SFWQQRLHEA EHKGLQGGRM TLVFGCRRPE
     EDHLYWEEML EMARKGVLHE VHTAYSRLPD QPKVYVQDIL RQRLAGEVLR VLHEEQGHLY
     VCGDVRMARD VARTLKQLMA TALSLNEEQV EDYFFQLKNQ KRYHEDIFGA VFPYEVKKDG
     AAGLPSNPRA PGAHRS
//